ReviewJournal of lipid research2015
Calcium-independent phospholipases A2 and their roles in biological processes and diseases.
Review in Journal of lipid research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 109 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
109 citing papers in PubMed, 192 citations in OpenAlex.
- Phospholipases: Where Do We Stand?Methods in molecular biology (Clifton, N.J.) · 2027Review
- The Phospholipase AJournal of lipid and atherosclerosis · 2026Review
- Phospholipase A2 Isoforms in Lung Immunity and Respiratory Infections: Potential Targets for Next-Generation Therapy.International journal of molecular sciences · 2026Review
- Pla2g6 Deficiency Induces Neuronal Precursor Apoptosis During Neurodevelopment.International journal of molecular sciences · 2026Article
- Xiebai San Alleviates Allergic Pulmonary Inflammation by Modulating Arachidonic Acid Metabolism.Pharmaceuticals (Basel, Switzerland) · 2026Article
- Specificity mechanism of Group VIA calcium-independent phospholipase ABiochimica et biophysica acta. Molecular and cell biology of lipids · 2025Article
- The balancing act between lipid droplets and lysosomes for membrane functionality in age-related neurodegeneration and inflammation.Progress in lipid research · 2025Review
- Natural variation in phospholipase IPLA2-VIA contributes to starvation sensitivity inbioRxiv : the preprint server for biology · 2025Article
- Insights from selenoprotein I mouse models for understanding biological roles of this enzyme.Archives of biochemistry and biophysics · 2025Review
- Association of Novel Pathogenic Variant (p. Ile366Asn) inInternational journal of molecular sciences · 2025Article
- Link between Parkinson's disease and melanoma: insights into the influence of theFrontiers in oncology · 2025Review
- Identifying potential biomarkers and molecular mechanisms related to arachidonic acid metabolism in vitiligo.Frontiers in molecular biosciences · 2025Article
- Novel PNPLA8 variants associated with primary ovarian insufficiency, tremors, cerebellar ataxia and limb weakness: a case report and literature review.Journal of neurology · 2024Review
- Differentiating human phospholipase ABiochimica et biophysica acta. Molecular and cell biology of lipids · 2024Article
- Rapid Movement of Palmitoleic Acid from Phosphatidylcholine to Phosphatidylinositol in Activated Human Monocytes.Biomolecules · 2024Article
- High patatin like phospholipase domain containing 8 expression as a biomarker for poor prognosis of colorectal cancer.World journal of gastrointestinal oncology · 2024Article
- Differential lipid signaling from CD4Frontiers in immunology · 2024Article
- A novel variant ofFrontiers in neurology · 2024Article
- Peripheral blood TCR clonotype diversity as an age-associated marker of breast cancer progression.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Key regulator PNPLA8 drives phospholipid reprogramming induced proliferation and migration in triple-negative breast cancer.Breast cancer research : BCR · 2023Article
49 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Among the family of phospholipases A2 (PLA2s) are the Ca(2+)-independent PLA2s (iPLA2s) and they are designated group VI iPLA2s. In relation to secretory and cytosolic PLA2s, the iPLA2s are more recently described and details of their expression and roles in biological functions are rapidly emerging. The iPLA2s or patatin-like phospholipases (PNPLAs) are intracellular enzymes that do not require Ca(2+) for activity, and contain lipase (GXSXG) and nucleotide-binding (GXGXXG) consensus sequences. Though nine PNPLAs have been recognized, PNPLA8 (membrane-associated iPLA2γ) and PNPLA9 (cytosol-associated iPLA2β) are the most widely studied and understood. The iPLA2s manifest a variety of activities in addition to phospholipase, are ubiquitously expressed, and participate in a multitude of biological processes, including fat catabolism, cell differentiation, maintenance of mitochondrial integrity, phospholipid remodeling, cell proliferation, signal transduction, and cell death. As might be expected, increased or decreased expression of iPLA2s can have profound effects on the metabolic state, CNS function, cardiovascular performance, and cell survival; therefore, dysregulation of iPLA2s can be a critical factor in the development of many diseases. This review is aimed at providing a general framework of the current understanding of the iPLA2s and discussion of the potential mechanisms of action of the iPLA2s and related involved lipid mediators.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.